Investigation of Osmolyte Effects on FolM: Comparison with Other Dihydrofolate Reductases
Author:
Affiliation:
1. Department of Biochemistry and Cellular and Molecular Biology, University of Tennessee, Knoxville, Tennessee 37996-0840, United States
Funder
National Science Foundation
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi4014165
Reference88 articles.
1. Role of Hydration in the Binding of lac Repressor to DNA
2. A Balancing Act between Net Uptake of Water during Dihydrofolate Binding and Net Release of Water upon NADPH Binding in R67 Dihydrofolate Reductase
3. Unusual Binding Stoichiometries and Cooperativity Are Observed during Binary and Ternary Complex Formation in the Single Active Pore of R67 Dihydrofolate Reductase, a D2 Symmetric Protein
4. Crystal Structure of a Type II Dihydrofolate Reductase Catalytic Ternary Complex
5. The stabilization of proteins by osmolytes
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